Detail of "258279-04-8"

Reference

Semisynthesis of human ghrelin: Condensation of a Boc-protected recombinant peptide with a synthetic O-acylated fragment

Semisynthesis of human ghrelin: Condensation of a Boc-protected recombinant peptide with a synthetic O-acylated fragment.Several substances are used for example 258279-04-8 which is its cas registry number. Makino, Tomohiro; Matsumoto, Masaru; Suzuki, Yuji; Kitajima, Yasuo; Yamamoto, Katsuhiko; Kuramoto, Masashi; Minamitake, Yoshiharu; Kangawa, Kenji; Yabuta, Masayuki (Institute for Medicinal Research and Development, Daiichi Suntory Pharma Co., Ltd., Chiyoda, Ohra, Gunma 370-0503, Japan). Biopolymers, 79(5), 238-247 (English) 2005 John Wiley & Sons, Inc. CODEN: BIPMAA.Several reagents such as 258279-04-8 is used here. ISSN: 0006-3525. DOCUMENT TYPE: Journal CA Section: 34 (Amino Acids, Peptides, and Proteins) Section cross-reference(s): 2 The creation of a peptide using a combination of recombinant expression and chem. synthesis can be a powerful tool for the prodn. of a wide variety of polypeptides modified by phosphorylation, glycosylation, etc. The authors have developed a new method for the prepn. of a recombinant peptide with a free Na-amino group and protected Ne-amino groups, and have used this method in the semisynthesis of human ghrelin. Ghrelin, a natural ligand for growth hormone secretagogue receptor, is a 28-residue peptide with an essential n-octanoyl modification on Ser3. A 7-residue N-terminal fragment of ghrelin contg. the octanoyl modification was prepd. by Fmoc chem. In the prepn. of it, all reactions were performed on the 2-chlorotrityl resin. Addnl., TBDMS (SiMe2Bu-t) and t-Bu turned out to be the most effective protection groups for the Ser3 and Ser2,6, resp. For prepn. of a 21-residue C-terminal fragment, the authors established a two-step protease processing method for the partially protected segment. A recombinant precursor peptide was Boc-protected and subsequently cleaved using two distinct proteases, OmpT and Kex2. The peptides were then coupled to each other and, after deprotection, resulted in fully active human ghrelin. ..

Semisynthesis of human ghrelin: Condensation of a Boc-protected recombinant peptide with a synthetic O-acylated fragment

Semisynthesis of human ghrelin: Condensation of a Boc-protected recombinant peptide with a synthetic O-acylated fragment.Several substances are used for example 258279-04-8 which is its cas registry number. Makino, Tomohiro; Matsumoto, Masaru; Suzuki, Yuji; Kitajima, Yasuo; Yamamoto, Katsuhiko; Kuramoto, Masashi; Minamitake, Yoshiharu; Kangawa, Kenji; Yabuta, Masayuki (Institute for Medicinal Research and Development, Daiichi Suntory Pharma Co., Ltd., Chiyoda, Ohra, Gunma 370-0503, Japan). Biopolymers, 79(5), 238-247 (English) 2005 John Wiley & Sons, Inc. CODEN: BIPMAA.Several reagents such as 258279-04-8 is used here. ISSN: 0006-3525. DOCUMENT TYPE: Journal CA Section: 34 (Amino Acids, Peptides, and Proteins) Section cross-reference(s): 2 The creation of a peptide using a combination of recombinant expression and chem. synthesis can be a powerful tool for the prodn. of a wide variety of polypeptides modified by phosphorylation, glycosylation, etc. The authors have developed a new method for the prepn. of a recombinant peptide with a free Na-amino group and protected Ne-amino groups, and have used this method in the semisynthesis of human ghrelin. Ghrelin, a natural ligand for growth hormone secretagogue receptor, is a 28-residue peptide with an essential n-octanoyl modification on Ser3. A 7-residue N-terminal fragment of ghrelin contg. the octanoyl modification was prepd. by Fmoc chem. In the prepn. of it, all reactions were performed on the 2-chlorotrityl resin. Addnl., TBDMS (SiMe2Bu-t) and t-Bu turned out to be the most effective protection groups for the Ser3 and Ser2,6, resp. For prepn. of a 21-residue C-terminal fragment, the authors established a two-step protease processing method for the partially protected segment. A recombinant precursor peptide was Boc-protected and subsequently cleaved using two distinct proteases, OmpT and Kex2. The peptides were then coupled to each other and, after deprotection, resulted in fully active human ghrelin. ..